2FSU
Crystal Structure of the PhnH Protein from Escherichia Coli
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X6A |
Synchrotron site | NSLS |
Beamline | X6A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-11-04 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.979029, 0.978681, 0.925256 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 53.020, 87.418, 75.890 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.920 - 1.700 |
R-factor | 0.19091 |
Rwork | 0.188 |
R-free | 0.24842 |
Structure solution method | MAD |
RMSD bond length | 0.029 |
RMSD bond angle | 2.308 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.770 |
High resolution limit [Å] | 1.570 | 1.570 |
Rmerge | 0.045 | 0.430 |
Number of reflections | 24912 | |
<I/σ(I)> | 42 | 2.8 |
Completeness [%] | 100.0 | 35.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 3.5 | 295 | magnesium acetate, PEG 4000, sodium citrate pH 3.5 with protein in HEPES buffer, VAPOR DIFFUSION, HANGING DROP, temperature 295K |